1G6Q
CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1
Summary for 1G6Q
| Entry DOI | 10.2210/pdb1g6q/pdb |
| Descriptor | HNRNP ARGININE N-METHYLTRANSFERASE (1 entity in total) |
| Functional Keywords | sam-binding domain, beta-barrel, mixed alpha-beta, hexamer, dimer, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 6 |
| Total formula weight | 226155.68 |
| Authors | Weiss, V.H.,McBride, A.E.,Soriano, M.A.,Filman, D.J.,Silver, P.A.,Hogle, J.M. (deposition date: 2000-11-07, release date: 2000-12-06, Last modification date: 2024-02-07) |
| Primary citation | Weiss, V.H.,McBride, A.E.,Soriano, M.A.,Filman, D.J.,Silver, P.A.,Hogle, J.M. The structure and oligomerization of the yeast arginine methyltransferase, Hmt1. Nat.Struct.Biol., 7:1165-1171, 2000 Cited by PubMed Abstract: Protein methylation at arginines is ubiquitous in eukaryotes and affects signal transduction, gene expression and protein sorting. Hmt1/Rmt1, the major arginine methyltransferase in yeast, catalyzes methylation of arginine residues in several mRNA-binding proteins and facilitates their export from the nucleus. We now report the crystal structure of Hmt1 at 2.9 A resolution. Hmt1 forms a hexamer with approximate 32 symmetry. The surface of the oligomer is dominated by large acidic cavities at the dimer interfaces. Mutation of dimer contact sites eliminates activity of Hmt1 both in vivo and in vitro. Mutating residues in the acidic cavity significantly reduces binding and methylation of the substrate Npl3. PubMed: 11101900DOI: 10.1038/78941 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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